[The carbohydrate specificity of the extracellular lectins in bacteria of the genus Bacillus].
The paper presents the study of interaction of extracellular sialo-specific lectins of Bacillus genus bacteria with different types of erythrocytes and affinity of these biologically active substances to derivatives of N-acetylneuramine acid and natural sialo and asialo conjugates. It is established that lectins under study possess a very narrow carbohydrate specificity and distinguish strictly definite carbohydrate structures. The identification processes first of all require the availability of N-glycolylneuraminic acid in the structure of receptors, and to the less extent of alpha-isomer of N-acetylneuraminic acid in O-acetylated form added to terminal galactose alpha 2-6-or alpha 2-3-bonds.
Kovalenko
E A
EA
D000818:Animals; D001407:Bacillus / Q000378:metabolism*; D001412:Bacillus subtilis / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism; D006168:Guinea Pigs; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D011817:Rabbits; D012795:Sialoglycoproteins / Q000378:metabolism
D001426:Bacterial Proteins; D037102:Lectins; D012795:Sialoglycoproteins
Uglevodnaia spetsifichnost' vnekletochnykh lektinov bakteriĭ roda Bacillus.